UniProtKB - P13395 (SPTCA_DROME)
Protein
Spectrin alpha chain
Gene
alpha-Spec
Organism
Drosophila melanogaster (Fruit fly)
Status
Functioni
Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization.3 Publications
Miscellaneous
Its transcript shares the first untranslated exon with the dlt transcript, suggesting a common regulation.
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Calcium bindingi | 2278 – 2289 | 1PROSITE-ProRule annotationAdd BLAST | 12 | |
Calcium bindingi | 2321 – 2332 | 2PROSITE-ProRule annotationAdd BLAST | 12 |
GO - Molecular functioni
- actin binding Source: FlyBase
- calcium ion binding Source: InterPro
- calmodulin binding Source: UniProtKB-KW
- microtubule binding Source: FlyBase
GO - Biological processi
- actin filament capping Source: UniProtKB-KW
- axon midline choice point recognition Source: FlyBase
- central nervous system development Source: FlyBase
- fusome organization Source: FlyBase
- germarium-derived female germ-line cyst formation Source: FlyBase
- germarium-derived oocyte fate determination Source: FlyBase
- long-term strengthening of neuromuscular junction Source: FlyBase
- maintenance of presynaptic active zone structure Source: FlyBase
- negative regulation of microtubule depolymerization Source: FlyBase
- neuromuscular synaptic transmission Source: FlyBase
- oocyte construction Source: FlyBase
- plasma membrane organization Source: FlyBase
- positive regulation of hippo signaling Source: FlyBase
- regulation of cell shape Source: UniProtKB-KW
- regulation of synapse organization Source: FlyBase
Keywordsi
Molecular function | Actin capping, Actin-binding, Calmodulin-binding |
Biological process | Cell shape |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-DME-264870, Caspase-mediated cleavage of cytoskeletal proteins R-DME-6798695, Neutrophil degranulation R-DME-6807878, COPI-mediated anterograde transport |
SignaLinki | P13395 |
Names & Taxonomyi
Protein namesi | Recommended name: Spectrin alpha chain |
Gene namesi | Name:alpha-Spec Synonyms:SPEC-A ORF Names:CG1977 |
Organismi | Drosophila melanogaster (Fruit fly) |
Taxonomic identifieri | 7227 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › |
Proteomesi |
|
Organism-specific databases
FlyBasei | FBgn0250789, alpha-Spec |
Subcellular locationi
Golgi apparatus
- Golgi apparatus 1 Publication
Cytoskeleton
- cytoskeleton 1 Publication
Note: Near the inner surface of the plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are found at the Golgi.
Cytoskeleton
- cytoskeleton Source: UniProtKB-SubCell
Golgi apparatus
- Golgi apparatus Source: FlyBase
Plasma Membrane
- apical plasma membrane Source: FlyBase
- basolateral plasma membrane Source: FlyBase
- lateral plasma membrane Source: FlyBase
- plasma membrane Source: FlyBase
Other locations
- cell cortex Source: FlyBase
- fusome Source: FlyBase
- neuromuscular junction Source: FlyBase
- spectrosome Source: FlyBase
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, Golgi apparatusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000073467 | 1 – 2415 | Spectrin alpha chainAdd BLAST | 2415 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1032 | Phosphoserine1 Publication | 1 | |
Modified residuei | 1034 | Phosphoserine2 Publications | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P13395 |
PRIDEi | P13395 |
PTM databases
iPTMneti | P13395 |
Expressioni
Tissue specificityi
A substantial pool of maternal protein in the egg undergoes dynamic changes in distribution early in embryogenesis. In gastrulated embryo, the highest level of protein is found in the respiratory tract cells and the lowest in parts of the forming gut.1 Publication
Developmental stagei
Expressed both maternally and zygotically.
Gene expression databases
Bgeei | FBgn0250789, Expressed in eye disc (Drosophila) and 56 other tissues |
ExpressionAtlasi | P13395, baseline and differential |
Genevisiblei | P13395, DM |
Interactioni
Subunit structurei
Native spectrin molecule is a tetramer composed of two antiparallel heterodimers joined head to head so that each end of the native molecule includes the C-terminus of the alpha subunit and the N-terminus of the beta subunit.
Interacts with calmodulin in a calcium-dependent manner, interacts with F-actin and also interacts with Lva.
Interacts with Ten-m.
2 PublicationsGO - Molecular functioni
- actin binding Source: FlyBase
- calmodulin binding Source: UniProtKB-KW
- microtubule binding Source: FlyBase
Protein-protein interaction databases
BioGRIDi | 63763, 46 interactors |
DIPi | DIP-17516N |
IntActi | P13395, 2 interactors |
STRINGi | 7227.FBpp0305100 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P13395 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P13395 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 48 – 150 | Spectrin 1Sequence analysisAdd BLAST | 103 | |
Repeati | 154 – 254 | Spectrin 2Sequence analysisAdd BLAST | 101 | |
Repeati | 258 – 362 | Spectrin 3Sequence analysisAdd BLAST | 105 | |
Repeati | 366 – 464 | Spectrin 4Sequence analysisAdd BLAST | 99 | |
Repeati | 471 – 574 | Spectrin 5Sequence analysisAdd BLAST | 104 | |
Repeati | 577 – 679 | Spectrin 6Sequence analysisAdd BLAST | 103 | |
Repeati | 683 – 784 | Spectrin 7Sequence analysisAdd BLAST | 102 | |
Repeati | 788 – 890 | Spectrin 8Sequence analysisAdd BLAST | 103 | |
Repeati | 894 – 963 | Spectrin 9Sequence analysisAdd BLAST | 70 | |
Domaini | 970 – 1029 | SH3PROSITE-ProRule annotationAdd BLAST | 60 | |
Repeati | 1079 – 1177 | Spectrin 10Sequence analysisAdd BLAST | 99 | |
Repeati | 1181 – 1284 | Spectrin 11Sequence analysisAdd BLAST | 104 | |
Repeati | 1287 – 1391 | Spectrin 12Sequence analysisAdd BLAST | 105 | |
Repeati | 1394 – 1496 | Spectrin 13Sequence analysisAdd BLAST | 103 | |
Repeati | 1500 – 1604 | Spectrin 14Sequence analysisAdd BLAST | 105 | |
Repeati | 1608 – 1710 | Spectrin 15Sequence analysisAdd BLAST | 103 | |
Repeati | 1714 – 1816 | Spectrin 16Sequence analysisAdd BLAST | 103 | |
Repeati | 1820 – 1921 | Spectrin 17Sequence analysisAdd BLAST | 102 | |
Repeati | 1926 – 2028 | Spectrin 18Sequence analysisAdd BLAST | 103 | |
Repeati | 2040 – 2141 | Spectrin 19Sequence analysisAdd BLAST | 102 | |
Repeati | 2154 – 2252 | Spectrin 20Sequence analysisAdd BLAST | 99 | |
Domaini | 2265 – 2300 | EF-hand 1PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 2308 – 2343 | EF-hand 2PROSITE-ProRule annotationAdd BLAST | 36 |
Sequence similaritiesi
Belongs to the spectrin family.Curated
Keywords - Domaini
Repeat, SH3 domainPhylogenomic databases
eggNOGi | KOG0040, Eukaryota |
GeneTreei | ENSGT00940000156662 |
HOGENOMi | CLU_000847_0_0_1 |
InParanoidi | P13395 |
OMAi | QQFNRTV |
PhylomeDBi | P13395 |
Family and domain databases
CDDi | cd00051, EFh, 1 hit cd11808, SH3_Alpha_Spectrin, 1 hit |
InterProi | View protein in InterPro IPR035825, Alpha_Spectrin_SH3 IPR011992, EF-hand-dom_pair IPR014837, EF-hand_Ca_insen IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom IPR036028, SH3-like_dom_sf IPR001452, SH3_domain IPR018159, Spectrin/alpha-actinin IPR002017, Spectrin_repeat |
Pfami | View protein in Pfam PF13499, EF-hand_7, 1 hit PF08726, EFhand_Ca_insen, 1 hit PF00018, SH3_1, 1 hit PF00435, Spectrin, 20 hits |
PRINTSi | PR00452, SH3DOMAIN |
SMARTi | View protein in SMART SM00054, EFh, 2 hits SM00326, SH3, 1 hit SM00150, SPEC, 20 hits |
SUPFAMi | SSF47473, SSF47473, 1 hit SSF50044, SSF50044, 1 hit |
PROSITEi | View protein in PROSITE PS00018, EF_HAND_1, 2 hits PS50222, EF_HAND_2, 2 hits PS50002, SH3, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
P13395-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ
60 70 80 90 100
YFKRDADELE SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN
110 120 130 140 150
AIVSLDNTGQ EMINQQHFAS ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ
160 170 180 190 200
ALVLVQFLRQ CEEVMFWIKD KETFVTADEF GQDLEHVEVL QRKFDEFQKD
210 220 230 240 250
MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW QRLKQLAIVR
260 270 280 290 300
QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH
310 320 330 340 350
EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT
360 370 380 390 400
TKARERKQKL DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE
410 420 430 440 450
ALLERHQEHK GEIDAREDSF KLTTESGQKL LEREHYAAAE IQEKLAALEN
460 470 480 490 500
DKSSLLSLWE DRRILYEQCM DLQLFYRDTE QADTWMAKQE AFLANEDLGD
510 520 530 540 550
SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ HYAADDVAQR
560 570 580 590 600
RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT
610 620 630 640 650
DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD
660 670 680 690 700
QINTRMQEIV VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI
710 720 730 740 750
EGQLLSEDHG KDLTSVQNLQ KKHALLEADV MAHQDRIESI KVAANKFIES
760 770 780 790 800
GHFDADNIRN KEGNLSARYA ALAAPMGERK QHLLDSLQVQ QLFRDLEDEA
810 820 830 840 850
AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE ARLLNVISSG
860 870 880 890 900
ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA
910 920 930 940 950
DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ
960 970 980 990 1000
ALQEQAKNCR QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL
1010 1020 1030 1040 1050
NSNNKDWWKV EVNDRQGFVP AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ
1060 1070 1080 1090 1100
INSQYDNLLA LARERQNKLN ETVKAYVLVR EAADLAQWIR DKENHAQIAD
1110 1120 1130 1140 1150
VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL TSLGQTEAAL
1160 1170 1180 1190 1200
KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK
1210 1220 1230 1240 1250
ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS
1260 1270 1280 1290 1300
HPDTAEQTYA KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL
1310 1320 1330 1340 1350
AWINSMMSLV TSDELANDVT GAEALIERHQ EHRTEIDARA GTFGAFEQFG
1360 1370 1380 1390 1400
NELLQANHYA SPEIKEKIED LAKAREDLEK AWTERRLQLE QNLDLQLYMR
1410 1420 1430 1440 1450
DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK AINGHEQKIA
1460 1470 1480 1490 1500
ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT
1510 1520 1530 1540 1550
LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN
1560 1570 1580 1590 1600
ADRIQSVLAM GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL
1610 1620 1630 1640 1650
KLKEANKQRT YIAAVKDLDF WLGEVESLLT TEDSGKDLAS VQNLMKKHQL
1660 1670 1680 1690 1700
VEADIVAHED RIKDMNNQAD SLVESGQFDT AGIQEKRQSI NERYERICNL
1710 1720 1730 1740 1750
AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY GRDLTGVQNL
1760 1770 1780 1790 1800
KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW
1810 1820 1830 1840 1850
AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM
1860 1870 1880 1890 1900
AAVQGLLKKH DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ
1910 1920 1930 1940 1950
QLRLKLDNLS ALAARRKGAL LDNSAYLQFM WKADVVESWI DDKENYVRSD
1960 1970 1980 1990 2000
EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG IHNITALKDQ LINASHAQSP
2010 2020 2030 2040 2050
AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL YLTFAKKASA
2060 2070 2080 2090 2100
FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA
2110 2120 2130 2140 2150
LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE
2160 2170 2180 2190 2200
NDKLRKEFAK HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR
2210 2220 2230 2240 2250
RVDLKKIEEL GALLEEHLIL DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL
2260 2270 2280 2290 2300
EQQIQARNHS GVSEDSLKEF SMMFKHFDKD KSGKLNHQEF KSCLRALGYD
2310 2320 2330 2340 2350
LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK ETENVQSYEE
2360 2370 2380 2390 2400
IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK
2410
DALDYIDFTR TLFQN
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketM9PBI5 | M9PBI5_DROME | Alpha spectrin, isoform C | alpha-Spec 3A9, alfa-Spec, alpha, alpha spectrin, alpha-Sp | 2,447 | Annotation score: | ||
M9PDQ0 | M9PDQ0_DROME | Alpha spectrin, isoform D | alpha-Spec 3A9, alfa-Spec, alpha, alpha spectrin, alpha-Sp | 2,425 | Annotation score: | ||
M9PGV6 | M9PGV6_DROME | Alpha spectrin, isoform B | alpha-Spec 3A9, alfa-Spec, alpha, alpha spectrin, alpha-Sp | 2,457 | Annotation score: |
Sequence cautioni
The sequence AAL39886 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence ABA81823 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 110 | Q → D in AAB29441 (PubMed:8276898).Curated | 1 | |
Sequence conflicti | 212 | N → I in ABA81823 (Ref. 4) Curated | 1 | |
Sequence conflicti | 337 | D → G in ABA81823 (Ref. 4) Curated | 1 | |
Sequence conflicti | 651 | Q → L in ABA81823 (Ref. 4) Curated | 1 | |
Sequence conflicti | 1555 | Q → H in AAL39886 (PubMed:12537569).Curated | 1 | |
Sequence conflicti | 1562 | G → E in ABA81823 (Ref. 4) Curated | 1 | |
Sequence conflicti | 1668 | Q → R in AAA28907 (PubMed:2808524).Curated | 1 | |
Sequence conflicti | 1908 | N → S in ABA81823 (Ref. 4) Curated | 1 | |
Sequence conflicti | 2203 | D → G in ABA81823 (Ref. 4) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M26400 mRNA Translation: AAA28907.1 AE014296 Genomic DNA Translation: AAF47569.1 BT023889 mRNA Translation: ABA81823.1 Frameshift. S67762 Genomic DNA Translation: AAB29441.2 S67765 Genomic DNA Translation: AAB29442.1 AY069741 mRNA Translation: AAL39886.1 Different initiation. |
PIRi | A33733 |
RefSeqi | NP_476739.1, NM_057391.4 |
Genome annotation databases
EnsemblMetazoai | FBtr0072789; FBpp0072672; FBgn0250789 |
GeneIDi | 38231 |
KEGGi | dme:Dmel_CG1977 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M26400 mRNA Translation: AAA28907.1 AE014296 Genomic DNA Translation: AAF47569.1 BT023889 mRNA Translation: ABA81823.1 Frameshift. S67762 Genomic DNA Translation: AAB29441.2 S67765 Genomic DNA Translation: AAB29442.1 AY069741 mRNA Translation: AAL39886.1 Different initiation. |
PIRi | A33733 |
RefSeqi | NP_476739.1, NM_057391.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2SPC | X-ray | 1.80 | A/B | 1391-1497 | [»] | |
SMRi | P13395 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 63763, 46 interactors |
DIPi | DIP-17516N |
IntActi | P13395, 2 interactors |
STRINGi | 7227.FBpp0305100 |
PTM databases
iPTMneti | P13395 |
Proteomic databases
PaxDbi | P13395 |
PRIDEi | P13395 |
Genome annotation databases
EnsemblMetazoai | FBtr0072789; FBpp0072672; FBgn0250789 |
GeneIDi | 38231 |
KEGGi | dme:Dmel_CG1977 |
Organism-specific databases
CTDi | 38231 |
FlyBasei | FBgn0250789, alpha-Spec |
Phylogenomic databases
eggNOGi | KOG0040, Eukaryota |
GeneTreei | ENSGT00940000156662 |
HOGENOMi | CLU_000847_0_0_1 |
InParanoidi | P13395 |
OMAi | QQFNRTV |
PhylomeDBi | P13395 |
Enzyme and pathway databases
Reactomei | R-DME-264870, Caspase-mediated cleavage of cytoskeletal proteins R-DME-6798695, Neutrophil degranulation R-DME-6807878, COPI-mediated anterograde transport |
SignaLinki | P13395 |
Miscellaneous databases
BioGRID-ORCSi | 38231, 0 hits in 3 CRISPR screens |
EvolutionaryTracei | P13395 |
GenomeRNAii | 38231 |
PROi | PR:P13395 |
Gene expression databases
Bgeei | FBgn0250789, Expressed in eye disc (Drosophila) and 56 other tissues |
ExpressionAtlasi | P13395, baseline and differential |
Genevisiblei | P13395, DM |
Family and domain databases
CDDi | cd00051, EFh, 1 hit cd11808, SH3_Alpha_Spectrin, 1 hit |
InterProi | View protein in InterPro IPR035825, Alpha_Spectrin_SH3 IPR011992, EF-hand-dom_pair IPR014837, EF-hand_Ca_insen IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom IPR036028, SH3-like_dom_sf IPR001452, SH3_domain IPR018159, Spectrin/alpha-actinin IPR002017, Spectrin_repeat |
Pfami | View protein in Pfam PF13499, EF-hand_7, 1 hit PF08726, EFhand_Ca_insen, 1 hit PF00018, SH3_1, 1 hit PF00435, Spectrin, 20 hits |
PRINTSi | PR00452, SH3DOMAIN |
SMARTi | View protein in SMART SM00054, EFh, 2 hits SM00326, SH3, 1 hit SM00150, SPEC, 20 hits |
SUPFAMi | SSF47473, SSF47473, 1 hit SSF50044, SSF50044, 1 hit |
PROSITEi | View protein in PROSITE PS00018, EF_HAND_1, 2 hits PS50222, EF_HAND_2, 2 hits PS50002, SH3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SPTCA_DROME | |
Accessioni | P13395Primary (citable) accession number: P13395 Secondary accession number(s): Q26340 Q9W085 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
Last sequence update: | June 20, 2001 | |
Last modified: | April 7, 2021 | |
This is version 212 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Drosophila annotation project |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Drosophila
Drosophila: entries, gene names and cross-references to FlyBase - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families